AB6B_ARATH
ID AB6B_ARATH Reviewed; 1407 AA.
AC Q8LPT1; O80635;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=ABC transporter B family member 6;
DE Short=ABC transporter ABCB.6;
DE Short=AtABCB6;
DE AltName: Full=Multidrug resistance protein 6;
DE AltName: Full=P-glycoprotein 6;
GN Name=ABCB6; Synonyms=MDR6, PGP6; OrderedLocusNames=At2g39480;
GN ORFNames=F12L6.14;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11346655; DOI=10.1074/jbc.m103104200;
RA Sanchez-Fernandez R., Davies T.G., Coleman J.O., Rea P.A.;
RT "The Arabidopsis thaliana ABC protein superfamily, a complete inventory.";
RL J. Biol. Chem. 276:30231-30244(2001).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18299247; DOI=10.1016/j.tplants.2008.02.001;
RA Verrier P.J., Bird D., Burla B., Dassa E., Forestier C., Geisler M.,
RA Klein M., Kolukisaoglu H.U., Lee Y., Martinoia E., Murphy A., Rea P.A.,
RA Samuels L., Schulz B., Spalding E.J., Yazaki K., Theodoulou F.L.;
RT "Plant ABC proteins - a unified nomenclature and updated inventory.";
RL Trends Plant Sci. 13:151-159(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255|PROSITE-ProRule:PRU00441};
CC Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Multidrug resistance exporter (TC 3.A.1.201) subfamily. {ECO:0000305}.
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DR EMBL; AC004218; AAC27839.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09685.1; -; Genomic_DNA.
DR EMBL; AY094398; AAM19777.1; -; mRNA.
DR PIR; T00558; T00558.
DR RefSeq; NP_181480.1; NM_129506.2.
DR AlphaFoldDB; Q8LPT1; -.
DR SMR; Q8LPT1; -.
DR BioGRID; 3871; 2.
DR IntAct; Q8LPT1; 2.
DR STRING; 3702.AT2G39480.1; -.
DR iPTMnet; Q8LPT1; -.
DR PaxDb; Q8LPT1; -.
DR PRIDE; Q8LPT1; -.
DR ProteomicsDB; 244627; -.
DR EnsemblPlants; AT2G39480.1; AT2G39480.1; AT2G39480.
DR GeneID; 818533; -.
DR Gramene; AT2G39480.1; AT2G39480.1; AT2G39480.
DR KEGG; ath:AT2G39480; -.
DR Araport; AT2G39480; -.
DR TAIR; locus:2039747; AT2G39480.
DR eggNOG; KOG0055; Eukaryota.
DR HOGENOM; CLU_000604_17_2_1; -.
DR InParanoid; Q8LPT1; -.
DR OrthoDB; 186078at2759; -.
DR PhylomeDB; Q8LPT1; -.
DR BioCyc; ARA:AT2G39480-MON; -.
DR PRO; PR:Q8LPT1; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8LPT1; baseline and differential.
DR Genevisible; Q8LPT1; AT.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR Gene3D; 1.20.1560.10; -; 3.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF90123; SSF90123; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1407
FT /note="ABC transporter B family member 6"
FT /id="PRO_0000227917"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 212..231
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 236..258
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 840..860
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 880..900
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 958..978
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 982..1002
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1061..1081
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1102..1122
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 86..379
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 412..647
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 835..1123
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1158..1395
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 18..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 447..454
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1193..1200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 663
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 727
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 767
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 58
FT /note="E -> G (in Ref. 3; AAM19777)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1407 AA; 155876 MW; 4148EA7252D9BCBA CRC64;
MMISRGLFGW SPPHIQPLTP VSEVSEPPES PSPYLDPGAE HGGTGTAAQA DDEEEMEEPE
EMEPPPAAVP FSQLFACADR FDWVLMVFGS VAAAAHGTAL IVYLHYFAKI VQVLAFPTDS
DHLISDDQFN RLLELSLTIV YIAGGVFISG WIEVSCWILT GERQTAVIRS KYVQVLLNQD
MSFFDTYGNN GDIVSQVLSD VLLIQSALSE KVGNYIHNMA TFISGLIIGF VNCWEIALIT
LATGPFIVAA GGISNIFLHR LAENIQDAYA EAASIAEQAV SYVRTLYAFT NETLAKYSYA
TSLQATLRYG ILISLVQGLG LGFTYGLAIC SCAMQLWIGR FFVIHHRANG GEIITALFAV
ILSGLGLNQA ATNFYSFDQG RIAAYRLFEM ISRSSSGTNQ EGIILSAVQG NIEFRNVYFS
YLSRPEIPIL SGFYLTVPAK KAVALVGRNG SGKSSIIPLM ERFYDPTLGE VLLDGENIKN
LKLEWLRSQI GLVTQEPALL SLSIRENIAY GRDATLDQIE EAAKKAHAHT FISSLEKGYE
TQVGKTGLTL TEEQKIKLSI ARAVLLDPTI LLLDEVTGGL DFEAERVVQE ALDLLMLGRS
TIIIARRLSL IRNADYIAVM EEGQLLEMGT HDELINLGNL YAELLKCEEA TKLPRRMPVR
NYNDSAAFQA ERDSSAGRGF QEPSSPKMAK SPSLQRGHNV FRSQELCFNS EESPNDHSPA
PEKLGENGSS LDVGEKEPTI KRQDSFEMRL PELPKIDIQC PQRQKSNGSD PESPISPLLI
SDPQNERSHS QTFSRPLGHS DDTSASVKVA KDGQHKEPPS FWRLAQLSFP EWLYAVLGSI
GAAIFGSFNP LLAYVIALVV TTYYTSKGSH LREEVDKWCL IIACMGIVTV VANFLQHFYF
GIMGEKMTER VRRMMFSAML RNEVGWYDEE ENSPDTLSMR LANDATFVRA AFSNRLSIFI
QDSFAVIVAI LIGLLLGWRL ALVALATLPV LTLSAIAQKL WLAGFSKGIQ EMHRKASLVL
EDAVRNIYTV VAFCAGNKVM ELYRLQLQRI LRQSFFHGMA IGFAFGFSQF LLFACNALLL
WYTALSVDRR YMKLSTALTE YMVFSFATFA LVEPFGLAPY ILKRRRSLAS VFEIIDRVPT
IEPDDTSALS PPNVYGSIEL KNIDFCYPTR PEVLVLSNFS LKVNGGQTVA VVGVSGSGKS
TIISLIERYY DPVAGQVLLD GRDLKSYNLR WLRSHMGLIQ QEPIIFSTTI RENIIYARHN
ASEAEMKEAA RIANAHHFIS SLPHGYDTHI GMRGVELTQG QKQRIAIARV VLKNAPILLI
DEASSSIESE SSRVVQEALD TLIMGNKTTI LIAHRVAMMR HVDNIVVLNG GKIVEEGTHD
CLAGKNGLYV RLMQPHFGKN LRRHQLI
